PROF2_PHLPR
ID PROF2_PHLPR Reviewed; 131 AA.
AC O24650;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Profilin-2;
DE AltName: Full=Allergen Phl p 11;
DE AltName: Full=Pollen allergen Phl p 12;
DE AltName: Full=Profilin 4;
DE AltName: Allergen=Phl p 12;
GN Name=PRO2;
GN and
GN Name=PRO4;
OS Phleum pratense (Common timothy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type); Poinae;
OC Phleum.
OX NCBI_TaxID=15957;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pollen;
RX PubMed=9224949; DOI=10.1016/s0167-4781(97)00061-4;
RA Asturias J.A., Arilla M.C., Bartolome B., Martinez J., Martinez A.,
RA Palacios R.;
RT "Sequence polymorphism and structural analysis of timothy grass pollen
RT profilin allergen (Phl p 11).";
RL Biochim. Biophys. Acta 1352:253-257(1997).
RN [2]
RP 3D-STRUCTURE MODELING, AND DISULFIDE BOND.
RX PubMed=24146818; DOI=10.1371/journal.pone.0076066;
RA Jimenez-Lopez J.C., Rodriguez-Garcia M.I., Alche J.D.;
RT "Analysis of the effects of polymorphism on pollen profilin structural
RT functionality and the generation of conformational, T- and B-cell
RT epitopes.";
RL PLoS ONE 8:E76066-E76066(2013).
CC -!- FUNCTION: Binds to actin and affects the structure of the cytoskeleton.
CC At high concentrations, profilin prevents the polymerization of actin,
CC whereas it enhances it at low concentrations. By binding to PIP2, it
CC inhibits the formation of IP3 and DG.
CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC actin in a 1:1 ratio.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Phosphorylated by MAP kinases. {ECO:0000250}.
CC -!- POLYMORPHISM: Several isoforms of the allergen exist due to
CC polymorphism.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC -!- MISCELLANEOUS: The variability of the residues taking part of IgE-
CC binding epitopes might be responsible of the difference in cross-
CC reactivity among olive pollen cultivars, and between distantly related
CC pollen species, leading to a variable range of allergy reactions among
CC atopic patients. {ECO:0000305|PubMed:24146818}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; Y09456; CAA70608.1; -; mRNA.
DR EMBL; Y09458; CAA70610.1; -; mRNA.
DR AlphaFoldDB; O24650; -.
DR SMR; O24650; -.
DR Allergome; 3490; Phl p 12.0102.
DR Allergome; 553; Phl p 12.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR CDD; cd00148; PROF; 1.
DR InterPro; IPR005455; PFN.
DR InterPro; IPR036140; PFN_sf.
DR InterPro; IPR027310; Profilin_CS.
DR PANTHER; PTHR11604; PTHR11604; 1.
DR Pfam; PF00235; Profilin; 1.
DR PRINTS; PR00392; PROFILIN.
DR PRINTS; PR01640; PROFILINPLNT.
DR SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; SSF55770; 1.
DR PROSITE; PS00414; PROFILIN; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Allergen; Cytoplasm; Cytoskeleton; Disulfide bond;
KW Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..131
FT /note="Profilin-2"
FT /id="PRO_0000199664"
FT MOTIF 81..97
FT /note="Involved in PIP2 interaction"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT DISULFID 13..115
FT /evidence="ECO:0000305|PubMed:24146818"
SQ SEQUENCE 131 AA; 14150 MW; 1B97B9DA084AE14C CRC64;
MSWQTYVDEH LMCEIEGHHL ASAAILGHDG TVWAQSADFP QFKPEEITGI MKDFDEPGHL
APTGMFVAGA KYMVIQGEPG AVIRGKKGAG GITIKKTGQA LVVGIYDEPM TPGQCNMVVE
RLGDYLVEQG M
